pubmed-article:11356138 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:11356138 | lifeskim:mentions | umls-concept:C0600464 | lld:lifeskim |
pubmed-article:11356138 | lifeskim:mentions | umls-concept:C0027021 | lld:lifeskim |
pubmed-article:11356138 | pubmed:issue | Pt 2 | lld:pubmed |
pubmed-article:11356138 | pubmed:dateCreated | 2001-5-17 | lld:pubmed |
pubmed-article:11356138 | pubmed:abstractText | Lignin peroxidase (LiP) and manganese peroxidase (MnP) have been investigated in Phanerochaete chrysosporium. A third ligninolytic peroxidase has been described in Pleurotus and Bjerkandera. Two of these versatile peroxidases (VPs) have been cloned, sequenced and characterized. They have high affinity for Mn(2+), hydroquinones and dyes, and also oxidize veratryl alcohol, dimethoxybenzene and lignin dimers. The deduced sequences show higher identity with Ph. chrysosporium LiP than MnP, but the molecular models obtained include a Mn(2+)-binding site. Concerning aromatic substrate oxidation, Pl. eryngii VP shows a putative long-range electron transfer pathway from an exposed trytophan to haem. Mutagenesis and chemical modification of this tryptophan and the acidic residues forming the Mn(2+)-binding site confirmed their role in catalysis. The existence of several substrate oxidation sites is supported further by biochemical evidence. Residue conservation in other fungal peroxidases is discussed. | lld:pubmed |
pubmed-article:11356138 | pubmed:language | eng | lld:pubmed |
pubmed-article:11356138 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11356138 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:11356138 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11356138 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11356138 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11356138 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11356138 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:11356138 | pubmed:month | May | lld:pubmed |
pubmed-article:11356138 | pubmed:issn | 0300-5127 | lld:pubmed |
pubmed-article:11356138 | pubmed:author | pubmed-author:MartínezM JMJ | lld:pubmed |
pubmed-article:11356138 | pubmed:author | pubmed-author:MartínezA TAT | lld:pubmed |
pubmed-article:11356138 | pubmed:author | pubmed-author:CamareroSS | lld:pubmed |
pubmed-article:11356138 | pubmed:author | pubmed-author:Ruiz-DueñasF... | lld:pubmed |
pubmed-article:11356138 | pubmed:author | pubmed-author:Pérez-BoadaMM | lld:pubmed |
pubmed-article:11356138 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:11356138 | pubmed:volume | 29 | lld:pubmed |
pubmed-article:11356138 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:11356138 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:11356138 | pubmed:pagination | 116-22 | lld:pubmed |
pubmed-article:11356138 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
pubmed-article:11356138 | pubmed:meshHeading | pubmed-meshheading:11356138... | lld:pubmed |
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pubmed-article:11356138 | pubmed:meshHeading | pubmed-meshheading:11356138... | lld:pubmed |
pubmed-article:11356138 | pubmed:year | 2001 | lld:pubmed |
pubmed-article:11356138 | pubmed:articleTitle | A new versatile peroxidase from Pleurotus. | lld:pubmed |
pubmed-article:11356138 | pubmed:affiliation | Centro de Investigaciones Biológicas, CSIC, Velázquez 144, E-28006 Madrid, Spain. | lld:pubmed |
pubmed-article:11356138 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:11356138 | pubmed:publicationType | Review | lld:pubmed |
pubmed-article:11356138 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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